| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2048436 | FEBS Letters | 2010 | 7 Pages |
Abstract
NfrA1 nitroreductase from the Gram-positive bacterium Bacillus subtilis is a member of the NAD(P)H/FMN oxidoreductase family. Here, we investigated the reactivity, the structure and kinetics of NfrA1, which could provide insight into the unclear biological role of this enzyme. We could show that NfrA1 possesses an NADH oxidase activity that leads to high concentrations of oxygen peroxide and an NAD+ degrading activity leading to free nicotinamide. Finally, we showed that NfrA1 is able to rapidly scavenge H2O2 produced during the oxidative process or added exogenously.Structured summaryMINT-7990140: nfrA1 (uniprotkb:P39605) and nfrA1 (uniprotkb:P39605) bind (MI:0407) by X-ray crystallography (MI:0114)
Related Topics
Life Sciences
Agricultural and Biological Sciences
Plant Science
Authors
Sylvie Cortial, Philippe Chaignon, Bogdan I. Iorga, Stéphane Aymerich, Gilles Truan, Virginie Gueguen-Chaignon, Philippe Meyer, Solange Moréra, Jamal Ouazzani,